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dc.contributor.supervisor Wieden, Hans-Joachim
dc.contributor.author De Laurentiis, Evelina I.
dc.contributor.author University of Lethbridge. Faculty of Arts and Science
dc.date.accessioned 2011-08-19T19:21:14Z
dc.date.available 2011-08-19T19:21:14Z
dc.date.issued 2009
dc.identifier.uri https://hdl.handle.net/10133/2515
dc.description xii, 127 leaves : ill. (some col.) ; 29 cm en_US
dc.description.abstract The translational GTPases elongation factor Tu (EF-Tu) and LepA modulate the dynamics of tRNA on the ribosome. EF-Tu facilitates the delivery of aminoacyl-tRNA (aa-tRNA) to the translating ribosome and LepA catalyzes the retro-translocation of tRNA•mRNA from the E- and P-sites of the ribosome back to the P- and A-sites. Although an increasing body of structural and biochemical information is available, little is known about the functional cycle of LepA during retro-translocation, the kinetics of EF-Tu dissociation from the ribosome and the rate of EF-Tu conformational change during aa-tRNA delivery. This thesis reports the successful construction and biochemical characterisation of a mutant form of EF-Tu from Escherichia coli ideal for the specific incorporation of fluorescent labels, enabling measurements pivotal for uncovering the rate of EF-Tu conformational change and dissociation from the ribosome. Furthermore, to determine structural components critical for LepA’s function, mutant versions of the protein were constructed and biochemically characterised. en_US
dc.language.iso en_US en_US
dc.publisher Lethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and Biochemistry, c2009 en_US
dc.relation.ispartofseries Thesis (University of Lethbridge. Faculty of Arts and Science) en_US
dc.subject Signal peptidases en_US
dc.subject Ribosomes -- Structure en_US
dc.subject Proteins -- Synthesis en_US
dc.subject G proteins en_US
dc.subject Dissertations, Academic en_US
dc.title Two partners of the ribosome, EF-Tu and LepA en_US
dc.type Thesis en_US
dc.publisher.faculty Arts and Science en_US
dc.publisher.department Department of Chemistry and Biochemistry en_US
dc.degree.level Masters


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